1pg1

About this Structure
1PG1 is a Single protein structure of sequence from Sus scrofa. Full experimental information is available from OCA. 1PG1 is an arginine and cysteine rich protein, which forms a double stranded anti-parallel β-sheet structure. The single chain forms a membrane-bound dimer, of structure 1ZY6. The structure of 1PG1 is similar to that of some other antimicrobial peptides such as defensins. In one study comparing the susceptibility of Chlamydia trachomatis to 1PG1 and a similar defensin peptide, 1PG1 was shown to be significantly more effective at inactivating the bacteria. The antimicrobial action of this protein is believed to be due to its ability to create pores in bacterial membranes causing ion leakage. This antimicrobial activity has given rise to the idea of using the peptide as a therapeutic for local or systemic infections.

Gene Ontology
Cellular Component Biological Process
 * extracellular region (GO:0005576)
 * defense response (GO:0006952)
 * defense response to bacterium (GO:0042742)

==SCOP Classification ==
 * Fold: Antimicrobial beta-hairpin
 * Superfamily: Antimicrobial beta-hairpin
 * Family: theta defensin-like

Reference
Solution structure of protegrin-1, a broad-spectrum antimicrobial peptide from porcine leukocytes., Fahrner RL, Dieckmann T, Harwig SS, Lehrer RI, Eisenberg D, Feigon J, Chem Biol. 1996 Jul;3(7):543-50. PMID:8807886

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